[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=3500856 [NCBI, ExPASy, EBI, Israel, Japan]
McKinnon C.M.,
Carter P.E.,
Smyth S.J.,
Dunbar B.,
Fothergill J.E.;
"Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence.";
Eur. J. Biochem. 169:547-553(1987).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00400a004; PubMed=2831944 [NCBI, ExPASy, EBI, Israel, Japan]
Tosi M.,
Duponchel C.,
Meo T.,
Julier C.;
"Complete cDNA sequence of human complement Cls and close physical linkage of the homologous genes Cls and Clr.";
Biochemistry 26:8516-8524(1987).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2459702 [NCBI, ExPASy, EBI, Israel, Japan]
Kusumoto H.,
Hirosawa S.,
Salier J.-P.,
Hagen F.S.,
Kurachi K.;
"Human genes for complement components C1r and C1s in a close tail-to-tail arrangement.";
Proc. Natl. Acad. Sci. U.S.A. 85:7307-7311(1988).
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=PNS;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[5]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-329.
TISSUE=Peripheral blood leukocyte;
PubMed=9794427 [NCBI, ExPASy, EBI, Israel, Japan]
Endo Y.,
Takahashi M.,
Nakao M.,
Saiga H.,
Sekine H.,
Matsushita M.,
Nonaka M.,
Fujita T.;
"Two lineages of mannose-binding lectin-associated serine protease (MASP) in vertebrates.";
J. Immunol. 161:4924-4930(1998).
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[6]
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NUCLEOTIDE SEQUENCE OF 291-688.
DOI=10.1016/0022-2836(89)90161-7; PubMed=2553984 [NCBI, ExPASy, EBI, Israel, Japan]
Tosi M.,
Duponchel C.,
Meo T.,
Couture-Tosi E.;
"Complement genes C1r and C1s feature an intronless serine protease domain closely related to haptoglobin.";
J. Mol. Biol. 208:709-714(1989).
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[7]
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PROTEIN SEQUENCE OF 16-61; 168-219; 287-334 AND 384-445.
PubMed=3007145 [NCBI, ExPASy, EBI, Israel, Japan]
Spycher S.E.,
Nick H.,
Rickli E.E.;
"Human complement component C1s. Partial sequence determination of the heavy chain and identification of the peptide bond cleaved during activation.";
Eur. J. Biochem. 156:49-57(1986).
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[8]
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PROTEIN SEQUENCE OF 438-500; 503-534; 542-601; 617-623 AND 626-656.
PubMed=6362661 [NCBI, ExPASy, EBI, Israel, Japan]
Carter P.E.,
Dunbar B.,
Fothergill J.E.;
"The serine proteinase chain of human complement component C1s. Cyanogen bromide cleavage and N-terminal sequences of the fragments.";
Biochem. J. 215:565-571(1983).
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[9]
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PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-174, AND HYDROXYLATION AT ASN-149.
DOI=10.1021/bi00466a021; PubMed=2141278 [NCBI, ExPASy, EBI, Israel, Japan]
Thielens N.M.,
van Dorsselaer A.,
Gagnon J.,
Arlaud G.J.;
"Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region.";
Biochemistry 29:3570-3578(1990).
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[10]
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PARTIAL PROTEIN SEQUENCE.
TISSUE=Plasma;
DOI=10.1021/bi00243a014; PubMed=1854725 [NCBI, ExPASy, EBI, Israel, Japan]
Illy C.,
Thielens N.M.,
Gagnon J.,
Arlaud G.J.;
"Effect of lactoperoxidase-catalyzed iodination on the Ca(2+)-dependent interactions of human C1s. Location of the iodination sites.";
Biochemistry 30:7135-7141(1991).
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[11]
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DISULFIDE BONDS.
DOI=10.1021/bi00225a014; PubMed=2007122 [NCBI, ExPASy, EBI, Israel, Japan]
Hess D.,
Schaller J.,
Rickli E.E.;
"Identification of the disulfide bonds of human complement C1s.";
Biochemistry 30:2827-2833(1991).
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[12]
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PARTIAL PROTEIN SEQUENCE, AND 3D-STRUCTURE MODELING OF CATALYTIC DOMAIN.
DOI=10.1021/bi00022a004; PubMed=7779774 [NCBI, ExPASy, EBI, Israel, Japan]
Rossi V.,
Gaboriaud C.,
Lacroix M.,
Ulrich J.,
Fontecilla-Camps J.-C.,
Gagnon J.,
Arlaud G.J.;
"Structure of the catalytic region of human complement protease C1s: study by chemical cross-linking and three-dimensional homology modeling.";
Biochemistry 34:7311-7321(1995).
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[13]
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DISEASE.
PubMed=11390518 [NCBI, ExPASy, EBI, Israel, Japan]
Dragon-Durey M.-A.,
Quartier P.,
Fremeaux-Bacchi V.,
Blouin J.,
de Barace C.,
Prieur A.-M.,
Weiss L.,
Fridman W.-H.;
"Molecular basis of a selective C1s deficiency associated with early onset multiple autoimmune diseases.";
J. Immunol. 166:7612-7616(2001).
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[14]
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GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-406, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T.,
Qian W.-J.,
Gritsenko M.A.,
Camp D.G. II,
Monroe M.E.,
Moore R.J.,
Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
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[15]
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X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 358-688.
DOI=10.1093/emboj/19.8.1755; PubMed=10775260 [NCBI, ExPASy, EBI, Israel, Japan]
Gaboriaud C.,
Rossi V.,
Bally I.,
Arlaud G.J.,
Fontecilla-Camps J.-C.;
"Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle.";
EMBO J. 19:1755-1765(2000).
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[16]
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X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 16-174, CALCIUM-BINDING SITES, AND GLYCOSYLATION AT ASN-406.
DOI=10.1074/jbc.M305175200; PubMed=12788922 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory L.A.,
Thielens N.M.,
Arlaud G.J.,
Fontecilla-Camps J.-C.,
Gaboriaud C.;
"X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement.";
J. Biol. Chem. 278:32157-32164(2003).
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